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2W7D

Crystal structure of Y51FbsSHMT internal aldimine

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004372molecular_functionglycine hydroxymethyltransferase activity
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006545biological_processglycine biosynthetic process
A0006730biological_processone-carbon metabolic process
A0008652biological_processamino acid biosynthetic process
A0016740molecular_functiontransferase activity
A0019264biological_processglycine biosynthetic process from serine
A0030170molecular_functionpyridoxal phosphate binding
A0035999biological_processtetrahydrofolate interconversion
A0046653biological_processtetrahydrofolate metabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues18
DetailsBINDING SITE FOR RESIDUE PLP A 501
ChainResidue
ASER93
AHIS225
ALYS226
AGLY256
AGLY257
AHOH2094
AHOH2279
AHOH2294
AHOH2429
AHOH2430
AGLY94
AALA95
AHIS122
ASER172
AASP197
AALA199
AHIS200
ATHR223

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE MPD A 601
ChainResidue
ATYR152
AARG156
AGLU185
AILE186
ALEU322
AHOH2244
AHOH2431
AHOH2432

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE PO4 A 701
ChainResidue
AGLU371
AHOH2394
AHOH2433

Functional Information from PROSITE/UniProt
site_idPS00096
Number of Residues17
DetailsSHMT Serine hydroxymethyltransferase pyridoxal-phosphate attachment site. HFvTTTTHKTLrGPRGG
ChainResidueDetails
AHIS218-GLY234

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PDB entries from 2024-11-06

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